3-D 'map' of enzyme could lead to more effective drugs

Scientists have completed a 3-D map of an enzyme that facilitates metabolism, an advance that could help develop more effective drugs.
Researchers have been studying enzymes for decades in order to learn how they work and how to create better drugs and medical treatments for many ailments.
Now, University of Missouri researchers have completed a 3-D map of an enzyme called Proline utilisation A (PutA) that facilitates metabolism by adding oxygen to molecules.
John Tanner, a professor in the MU Department of Biochemistry, said mapping this enzyme will give researchers a better understanding of its function, which could help drug manufacturers create more effective drugs.

"PutA is actually two enzymes fused together to make its processing more efficient," Tanner said.
"Now that we have an understanding about how PutA is constructed, we can study exactly how it works. Some dangerous bacteria, such as h pylori, which infect stomach tissue, utilise the PutA enzyme to grow.

"Discovering the structure of this enzyme will provide valuable insight into how this protein functions and could provide blueprints for designing drugs that inhibit or increase certain protein functions, which would make those drugs more effective," Tanner said.
Tanner conducted his study by using a process called protein crystallography. This process involves growing microscopic crystals made of PutA enzymes.

Tanner then shipped the protein crystals to Berkeley, California, where they were exposed to a high-powered X-ray device called a "beamline."
The beamline captures X-rays, focuses them on protein crystals, and records the beams that reflect or "diffract" off the crystals.
Tanner decoded the diffraction patterns from his crystals to understand the precise arrangement of the atoms in the protein and created a 3-D "map" of the PutA enzyme.
The study was published in the journal PNAS.